The Conformation of the ε- and γ-Subunits within the Escherichia coli F1 ATPase

Andrew C. Hausrath, Roderick A. Capaldi, Brian W. Matthews

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56 Scopus citations


F1 is the water-soluble portion of the ubiquitous F 1F0 ATP synthase. Its structure includes three α- and three β-subunits, arranged as a hexameric disc, plus a γ-subunit that penetrates the center of the disc akin to an axle. Recently Hausrath et al. (Hausrath, A. C., Grüber, G., Matthews, B. W., and Capaldi, R. A. (1999) Proc. Natl. Acad. Sci. U. S. A. 96, 13697-13702) obtained an electron density map of E. coli F1 at 4.4-Å resolution in which the coiled-coil α-helices of the γ-subunit could be seen to extend 45 Å from the base of the α3β3 hexamer. Subsequently the structure of a truncated form of the E. coli γ-subunit in complex with ε has been described (Rodgers, A. J. W., and Wilce, M. C. J. (2000) Nat. Struct. Biol. 7, 1051-1054). In the present study the 4.4-Å resolution electron density map of E. coli F1 is re-evaluated in light of the newly available data on the γ- and ε-subunits. It is shown that the map of the F1 complex is consistent with the structure of the isolated subunits. When E. coli F1 is compared with that from beef heart, the structures of the E. coli γ- and ε-subunits are seen to be generally similar to their counterparts in the bovine enzyme but to undergo major shifts in position. In particular, the two long, coiled-coil α-helices that lie along the axis of F1 both unwind and rotate. Also the ε-subunit rotates around the axis by 81° and undergoes a net translation of about 23 Å. It is argued that these large-scale changes in conformation reflect distinct functional states that occur during the rotation of the γ-subunit within the α3β3 hexamer.

Original languageEnglish (US)
Pages (from-to)47227-47232
Number of pages6
JournalJournal of Biological Chemistry
Issue number50
StatePublished - Dec 14 2001
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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